PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19770592-0 2009 Hexokinase II detachment from the mitochondria potentiates cisplatin induced cytotoxicity through a caspase-2 dependent mechanism. Cisplatin 59-68 caspase 2 Homo sapiens 100-109 19770592-4 2009 The present study demonstrates that cisplatin induces the PIDD (p53 induced protein with a death domain) dependent activation of caspase-2. Cisplatin 36-45 caspase 2 Homo sapiens 129-138 19770592-6 2009 Notably, the detachment of hexokinase II from the mitochondria markedly potentiates the onset of caspase-2 induced mitochondrial damage, thus resulting in a synergistic induction of cisplatin induced cytotoxicity. Cisplatin 182-191 caspase 2 Homo sapiens 97-106 16872918-3 2006 In this substrate, the sequence VDVAD could be specifically recognized and cleaved by caspase-2 as soon as its activation was initiated with treatment of a certain dose of cisplatin to HeLa cells, which led to a break of the substrate into two fragments. Cisplatin 172-181 caspase 2 Homo sapiens 86-95 18064041-5 2008 In the absence of functional p53, cisplatin treatment resulted in caspase-2-independent mitotic catastrophe followed by necrosis. Cisplatin 34-43 caspase 2 Homo sapiens 66-75 20009298-9 2009 Furthermore, we show that cisplatin treatment after the induction of UPR/GRP78 is facilitating the mitochondria-mediated apoptotic cascades through the initial activation of caspase-2 and down-regulation of genes involved in DNA repair. Cisplatin 26-35 caspase 2 Homo sapiens 174-183 18375382-5 2008 Under conditions when the expression of endogenous c-Myc, caspase-2, or Apaf-1 is reduced 80-90%, cisplatin (or etoposide)-induced apoptosis is significantly decreased. Cisplatin 98-107 caspase 2 Homo sapiens 58-67 16674201-0 2006 Real-time detection of caspase-2 activation in a single living HeLa cell during cisplatin-induced apoptosis. Cisplatin 80-89 caspase 2 Homo sapiens 23-32 16622172-0 2006 Caspases and calpain are independent mediators of cisplatin-induced endothelial cell necrosis. Cisplatin 50-59 caspase 2 Homo sapiens 0-8 16622172-8 2006 In conclusion, in cisplatin-treated endothelial cells, caspases, the major mediators of apoptosis, can also cause necrosis. Cisplatin 18-27 caspase 2 Homo sapiens 55-63 16674201-4 2006 Using these probes, we found that during cisplatin-induced apoptosis, caspase-2 activation occurred more slowly than did activation of caspase-3; additionally, caspase-2 activation was initiated much earlier than that of caspase-3. Cisplatin 41-50 caspase 2 Homo sapiens 70-79 16674201-4 2006 Using these probes, we found that during cisplatin-induced apoptosis, caspase-2 activation occurred more slowly than did activation of caspase-3; additionally, caspase-2 activation was initiated much earlier than that of caspase-3. Cisplatin 41-50 caspase 2 Homo sapiens 160-169 15492260-5 2004 Treatment with cisplatin, camptothecin, etoposide, betulinic acid, celecoxib, 1400W, and staurosporine promoted enzymatic activity not only of caspases -2, -8, and -3 but also of caspase-9 in both APAF-1(+) and APAF-1(-) tumor cells. Cisplatin 15-24 caspase 2 Homo sapiens 143-166 15983031-1 2005 We demonstrate the role of p53-mediated caspase-2 activation in the mitochondrial release of apoptosis-inducing factor (AIF) in cisplatin-treated renal tubular epithelial cells. Cisplatin 128-137 caspase 2 Homo sapiens 40-49 15983031-5 2005 Caspase-2 and -3 that were predominantly activated in response to cisplatin provided a unique model to study the role of these caspases in AIF release. Cisplatin 66-75 caspase 2 Homo sapiens 0-16 15983031-5 2005 Caspase-2 and -3 that were predominantly activated in response to cisplatin provided a unique model to study the role of these caspases in AIF release. Cisplatin 66-75 caspase 2 Homo sapiens 127-135 15983031-6 2005 Cisplatin-treated caspase-3 (+/+) and caspase-3 (-/-) cells exhibited similar AIF translocation to the nuclei, suggesting that caspase-3 does not affect AIF translocation, and thus, caspase-2 may be involved in the translocation. Cisplatin 0-9 caspase 2 Homo sapiens 182-191 15983031-8 2005 Caspase-2 activation was a critical response from p53, which was markedly induced and phosphorylated in cisplatin-treated cells. Cisplatin 104-113 caspase 2 Homo sapiens 0-9 15983031-10 2005 The p53 inhibitor pifithrin-alpha or p53 siRNA prevented both cisplatin-induced caspase-2 activation and mitochondrial release of AIF. Cisplatin 62-71 caspase 2 Homo sapiens 80-89 15983031-11 2005 Caspase-2 activation was dependent on the p53-responsive gene, PIDD, a death domain-containing protein that was induced by cisplatin in a p53-dependent manner. Cisplatin 123-132 caspase 2 Homo sapiens 0-9 15983031-12 2005 These results suggest that caspase-2 activation mediated by p53 is an important pathway involved in the mitochondrial release of AIF in response to cisplatin injury. Cisplatin 148-157 caspase 2 Homo sapiens 27-36 15455353-5 2005 Moreover, cisplatin-triggered activation of caspases 2 and 3 is potentiated upon expression of LMP1. Cisplatin 10-19 caspase 2 Homo sapiens 44-60 12373288-4 2002 Although both TNF and cisplatin caused activation of caspases, PKC modulators had opposing effects on caspase activation. Cisplatin 22-31 caspase 2 Homo sapiens 53-61 12373288-4 2002 Although both TNF and cisplatin caused activation of caspases, PKC modulators had opposing effects on caspase activation. Cisplatin 22-31 caspase 2 Homo sapiens 53-60 12373288-5 2002 Rottlerin inhibited mitochondrial or intrinsic cell death pathway by inhibiting cisplatin-induced processing of apical caspase-9 and its downstream caspases. Cisplatin 80-89 caspase 2 Homo sapiens 148-156 10194341-0 1999 Regulation of caspase activation and cis-diamminedichloroplatinum(II)-induced cell death by protein kinase C. Activation of caspases is critical for the induction of apoptosis. Cisplatin 37-69 caspase 2 Homo sapiens 124-132 10394958-0 1999 Up-regulation of ICH-1L protein by thromboxane A2 antagonists enhances cisplatin-induced apoptosis in non-small-cell lung-cancer cell lines. Cisplatin 71-80 caspase 2 Homo sapiens 17-23 10394958-7 1999 Ice and Ced-3 homolog (ICH-1L) expression was significantly lower in PC-9/CDDP and was up-regulated by S-1452 or ONO-NT-126. Cisplatin 74-78 caspase 2 Homo sapiens 23-29 10394958-8 1999 These data suggest that ICH-1L might play a critical role in cisplatin-induced apoptosis and that TXA2 blockade up-regulates ICH-1L protein expression. Cisplatin 61-70 caspase 2 Homo sapiens 24-30 30111833-5 2018 The detection of caspases and their cleavage products in the nucleus occurred within the same time interval after cisplatin treatment and took place shortly before nuclear fragmentation. Cisplatin 114-123 caspase 2 Homo sapiens 17-25 30816202-5 2019 In addition, miR-494 promoted the proliferation and colony formation of NSCLC cells and reduced their sensitivity to cisplatin-induced apoptosis by targeting CASP2. Cisplatin 117-126 caspase 2 Homo sapiens 158-163 27193717-1 2016 The mechanism of caspase-2 activation in response to DNA damage was studied using human ovarian cancer cells Caov-4 treated with chemotherapeutic agent cisplatin. Cisplatin 152-161 caspase 2 Homo sapiens 17-26